ID A0A8C9GRA8_9PRIM Unreviewed; 840 AA.
AC A0A8C9GRA8;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Coronin {ECO:0000256|RuleBase:RU280818};
GN Name=CORO7 {ECO:0000313|Ensembl:ENSPTEP00000008331.1};
OS Piliocolobus tephrosceles (Ugandan red Colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Piliocolobus.
OX NCBI_TaxID=591936 {ECO:0000313|Ensembl:ENSPTEP00000008331.1, ECO:0000313|Proteomes:UP000694416};
RN [1] {ECO:0000313|Ensembl:ENSPTEP00000008331.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSPTEP00000008331.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: F-actin regulator involved in anterograde Golgi to endosome
CC transport: upon ubiquitination via 'Lys-33'-linked ubiquitin chains by
CC the BCR(KLHL20) E3 ubiquitin ligase complex, interacts with EPS15 and
CC localizes to the trans-Golgi network, where it promotes actin
CC polymerization, thereby facilitating post-Golgi trafficking. May play a
CC role in the maintenance of the Golgi apparatus morphology.
CC {ECO:0000256|ARBA:ARBA00024838}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the WD repeat coronin family.
CC {ECO:0000256|ARBA:ARBA00009482, ECO:0000256|RuleBase:RU280818}.
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DR AlphaFoldDB; A0A8C9GRA8; -.
DR Ensembl; ENSPTET00000012714.1; ENSPTEP00000008331.1; ENSPTEG00000009393.1.
DR Proteomes; UP000694416; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:UniProtKB-ARBA.
DR FunFam; 2.130.10.10:FF:000076; Coronin; 1.
DR FunFam; 2.130.10.10:FF:001013; Coronin; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR015505; Coronin.
DR InterPro; IPR015048; DUF1899.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR10856; CORONIN; 1.
DR PANTHER; PTHR10856:SF20; CORONIN-7; 1.
DR Pfam; PF08953; DUF1899; 2.
DR Pfam; PF00400; WD40; 4.
DR Pfam; PF16300; WD40_4; 2.
DR SMART; SM01166; DUF1899; 2.
DR SMART; SM01167; DUF1900; 2.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; WD40 repeat-like; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000694416};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280818};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 3..64
FT /note="DUF1899"
FT /evidence="ECO:0000259|SMART:SM01166"
FT DOMAIN 381..446
FT /note="DUF1899"
FT /evidence="ECO:0000259|SMART:SM01166"
FT REPEAT 505..542
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 548..589
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 110..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..375
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..797
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..811
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 840 AA; 91675 MW; F981FFF36B341947 CRC64;
MNRFRVSKFR HTEARPPRRE AWISDIRAGT APSCRNHIKS SCSLIAFNSD HPGVLGIVPL
QGQGEDKRRV AHLGCHSELV AHGDLVQSAI WSRDGALVGT ACKDKQLRIF DPRTKPQASQ
STQAHENGRD SRLAWTGSRE HLVSTGFNQM REHEVKLWDT RVFSNALASL TLDTSPGCLM
PLLDPDSGLL VLAGKGERQL YCYEVVPQQP ALSPVTQCVL ESVLRGAALV PRQALAVMSC
EVLRVLQLSD TAIVPIGYHV PRKSVEFHED LFPDTAGCVP ATDPHSWWAG DNQQVQKVSL
NPACRPHPSF TSRLVPSMEP LPDTAQPAVM ETPAGDVDAS EGFSSPPSSL TSPSTPSSLG
PSLSSTSGIG TSPSLRSLQS LLGPSSKFRH AQGTVLHRDS HITNLKGLNL TTPGESDGFC
ANKLRVAVPL LSNGGQVAVL ELRKPGRLPD TALPTLQNGA AVTDLAWDPF DPHRLAVAGE
DARIRLWRVP PQGLEEVLTT PETVLTGHTE KICSLRFHPL AADVLASSSY DLTVRIWDLQ
AGVDRLKLQG HQDQIFSLAW SPDGQQLATV CKDGCVRIYR PRSGPEPLQE GPGPKGGRGA
RIVWVCDGRC LLVSGFDSQS ERQLLLYEAE ALAGGPLAVL GLDVAPSTLL PSYDPDTGLV
LLTGKGDTRV FLYELLPESP FFLECNSFTS PDPHKGFVLL PKTECDVREV ELMRCLRLRQ
SSLEPVAFRL PRVRKEFFQD DVFPDTAVSW EPVLSAEAWL QGANGQPWLL SLQPPDMSPV
SQAPREAPAR RAPSSAQYLE EKSDQQKKEE LLNAMVAKLG NREDPLPQDS FEGVDEDEWD
//
